Summary for 9JZ0
| Entry DOI | 10.2210/pdb9jz0/pdb |
| EMDB information | 61911 |
| Descriptor | Internal virion protein gp14, Protein 6.7, Portal protein, ... (6 entities in total) |
| Functional Keywords | complex, viral protein |
| Biological source | Escherichia phage T7 (Bacteriophage T7) More |
| Total number of polymer chains | 66 |
| Total formula weight | 2862416.12 |
| Authors | Liu, H.R.,Chen, W.Y. (deposition date: 2024-10-13, release date: 2024-12-11, Last modification date: 2025-06-25) |
| Primary citation | Zheng, J.,Xiao, H.,Pang, H.,Wang, L.,Song, J.,Chen, W.,Cheng, L.,Liu, H. Conformational changes in and translocation of small proteins: insights into the ejection mechanism of podophages. J.Virol., 99:e0124924-e0124924, 2025 Cited by PubMed Abstract: Podophage tails are too short to span the cell envelope during infection. Consequently, podophages initially eject the core proteins within the head for the formation of an elongated trans-envelope channel for DNA ejection. Although the core proteins of bacteriophage T7 have been resolved at near-atomic resolution, the mechanisms of core proteins and DNA ejection remain to be fully elucidated. In this study, we provided improved structures of core proteins in mature T7 and the portal-tail complex in lipopolysaccharide-induced DNA-ejected T7 to resolutions of approximately 3 Å. Using these structures, we identified three small proteins, namely gp14, gp6.7, and gp7.3, and illustrated the conformational changes in and translocation of these proteins from the mature to DNA-ejected states. Our structures indicate that gp6.7, which participates in the assembly of the core and trans-envelope channel, is a core protein, and that gp7.3 serves as a structural scaffold to assist the assembly of the nozzle into the adaptor. PubMed: 39704524DOI: 10.1128/jvi.01249-24 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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